Aspects of the mechanism of catalysis of glucose oxidase: A docking, molecular mechanics and quantum chemical study

Journal of Computer-Aided Molecular Design

Volumn 12, Issue 5, 1998, Pages 425-440

  Meyer, Michael ^a   Wohlfahrt, Gerd ^b,d   Knäblein, Jörg ^c,e   Schomburg, Dietmar ^c,f  

^a FRITZ LIPMANN INSTITUTE   (Germany)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^c Molekulare Strukturforschung   (Germany)

^d VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

^e MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^f UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Enzyme mechanism; Flavoenzyme; Force field; Ligand docking; QM MM; Semiempirical calculation

Indexed keywords

AMINO ACIDS; CATALYTIC OXIDATION; CONTINUUM MECHANICS; GLUCOSE OXIDASE; GLUCOSE SENSORS; MOLECULAR DYNAMICS; QUANTUM CHEMISTRY; REACTION KINETICS; REDOX REACTIONS; SOLVENTS; STABILIZATION;

ACTIVE-SITE MODELING; ENZYME MECHANISM; FLAVOENZYMES; FORCEFIELDS; HALF-REACTIONS; LIGAND DOCKING; QM/MM; QUANTUM CHEMICAL STUDIES; SEMI-EMPIRICAL CALCULATION; SUBSTRATE-BINDING;

GLUCOSE;

GLUCOSE OXIDASE; OXYGEN; SOLVENT;

ARTICLE; ASPERGILLUS NIGER; BINDING SITE; CATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; PROTEIN CONFORMATION; THERMODYNAMICS;

ASPERGILLUS NIGER; BINDING SITES; CATALYSIS; GLUCOSE OXIDASE; OXYGEN; PROTEIN CONFORMATION; SOLVENTS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 0032151412     PISSN: 0920654X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008020124326     Document Type: Article

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